Construction of a structural variant of sublancin to...

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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C514S009100, C530S300000, C530S317000, C530S324000, C530S825000

Reexamination Certificate

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06846804

ABSTRACT:
A sublancin peptide variant having a Gly-His peptide sequence fused to the C-terminal end of the mature sublancin peptide provides an affinity tag facilitating increased purification of the peptide variant from sample preparations without affecting the intracellular processing of the sublancin peptide variant, expression by a host cell or its biological activity in secreted form. This sublancin variant has specific inhibitory activity for spore outgrowth as for the native sublancin peptide. Production of the sublancin peptide variant on an industrial scale is set forth as are methods of decontaminating spore-infected areas. Methods for generating the peptide variant gene, plasmid and transformant are also described.

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patent: WO 0039152 (2000-07-01), None
Paik et al. 1998. Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced byBacillus subtilis168. J. Biol. Chem. 273:23134-23142.*
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Inglesby et al. 1999 Anthrax as a biological weapon: Medical and Public Health Management. JAMA (Journal of the American Medical Association) 281 (18): 1735-1745.*
Kupke et al. 1997. In vivo reaction of affinity tag labelled epidermin precursor peptide with flavoenzyme EpiD. FEMS Microbiology Letters 153:25-32.*
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